ReP USP - Resultado da busca

Artigo de periodico
Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis (2021)
Veldman, Wayde ; Liberato, Marcelo Vizoná; Souza, Valquiria P; Almeida, Vitor M; Marana, Sandro Roberto ; Bishop, Ozlem Tastan ; Polikarpov, Igor
Source: Journal of Chemical Information and Modeling. Unidades: IQ, IFSC
Subjects: CRISTALOGRAFIA, PEPTÍDEOS, PROTEÍNAS, LIGANTES
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ABNT
VELDMAN, Wayde et al. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, v. 61, n. 9, p. 4554-4570, 2021Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.1c00413. Acesso em: 16 nov. 2024.
APA
Veldman, W., Liberato, M. V., Souza, V. P., Almeida, V. M., Marana, S. R., Bishop, O. T., & Polikarpov, I. (2021). Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, 61( 9), 4554-4570. doi:10.1021/acs.jcim.1c00413
NLM
Veldman W, Liberato MV, Souza VP, Almeida VM, Marana SR, Bishop OT, Polikarpov I. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 9): 4554-4570.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.1c00413
Vancouver
Veldman W, Liberato MV, Souza VP, Almeida VM, Marana SR, Bishop OT, Polikarpov I. Differences in gluco and galacto substrate-binding interactions in a dual 6Pβ-Glucosidase/6Pβ-Galactosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2021 ; 61( 9): 4554-4570.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.1c00413
Artigo de periodico
Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes (2021)
Vignoni, Alejandro ; Layana, Carla; Junqueira, Helena Couto; Thomas, Andrés H.; Itri, Rosangela ; Baptista, Maurício da Silva ; Vignoni, Mariana
Source: Dyes and Pigments. Unidades: IF, IQ
Subjects: BIOFÍSICA, FÍSICO-QUÍMICA, MEMBRANAS CELULARES, FOTOSSENSIBILIZAÇÃO EM ANIMAL
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ABNT
VIGNONI, Alejandro et al. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes. Dyes and Pigments, v. 187, 2021Tradução . . Disponível em: https://doi.org/10.1016/j.dyepig.2020.109131. Acesso em: 16 nov. 2024.
APA
Vignoni, A., Layana, C., Junqueira, H. C., Thomas, A. H., Itri, R., Baptista, M. da S., & Vignoni, M. (2021). Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes. Dyes and Pigments, 187. doi:10.1016/j.dyepig.2020.109131
NLM
Vignoni A, Layana C, Junqueira HC, Thomas AH, Itri R, Baptista M da S, Vignoni M. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes [Internet]. Dyes and Pigments. 2021 ; 187[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.dyepig.2020.109131
Vancouver
Vignoni A, Layana C, Junqueira HC, Thomas AH, Itri R, Baptista M da S, Vignoni M. Alkylation of a hydrophilic photosensitizer enhances the contact-dependent photo-induced oxidation of phospholipid membranes [Internet]. Dyes and Pigments. 2021 ; 187[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.dyepig.2020.109131
Artigo de periodico
X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis (2020)
Veldman, Wayde ; Liberato, Marcelo Vizoná; Almeida, Vitor Medeiros ; Souza, Valquiria P; Frutuoso, Maira Artischeff; Marana, Sandro Roberto ; Moses, Vuyani; Bishop, Ozlem Tastan; Polikarpov, Igor
Source: Journal of Chemical Information and Modeling. Unidades: IQ, IFSC, FO
Subjects: RAIOS X, BIOINFORMÁTICA
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ABNT
VELDMAN, Wayde et al. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, v. 60, n. 12, p. 6392-6407, 2020Tradução . . Disponível em: https://doi.org/10.1021/acs.jcim.0c00759. Acesso em: 16 nov. 2024.
APA
Veldman, W., Liberato, M. V., Almeida, V. M., Souza, V. P., Frutuoso, M. A., Marana, S. R., et al. (2020). X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis. Journal of Chemical Information and Modeling, 60( 12), 6392-6407. doi:10.1021/acs.jcim.0c00759
NLM
Veldman W, Liberato MV, Almeida VM, Souza VP, Frutuoso MA, Marana SR, Moses V, Bishop OT, Polikarpov I. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6392-6407.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.0c00759
Vancouver
Veldman W, Liberato MV, Almeida VM, Souza VP, Frutuoso MA, Marana SR, Moses V, Bishop OT, Polikarpov I. X-ray structure, bioinformatics analysis, and substrate specificity of a 6-phospho-β-glucosidase glycoside hydrolase 1 enzyme from Bacillus licheniformis [Internet]. Journal of Chemical Information and Modeling. 2020 ; 60( 12): 6392-6407.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1021/acs.jcim.0c00759
Artigo de periodico
The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis (2020)
Sastre, Diego Emiliano; Pulschen, Andre A; Basso, Luís Guilherme Mansor; Pariente, Jhonathan Stivins Benites; Marques Netto, Caterina Gruenwaldt Cunha; Machinandiarena, Federico; Albanesi, Daniela; Navarro, Marcos Vicente de Albuquerque Salles ; Mendoza, Diego de; Gueiros Filho, Frederico José
Source: Journal of Biological Chemistry. Unidades: IFSC, IQ, FFCLRP
Subjects: BACTÉRIAS GRAM-POSITIVAS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano et al. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, v. 295, n. 7, p. 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011147. Acesso em: 16 nov. 2024.
APA
Sastre, D. E., Pulschen, A. A., Basso, L. G. M., Pariente, J. S. B., Marques Netto, C. G. C., Machinandiarena, F., et al. (2020). The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis. Journal of Biological Chemistry, 295( 7), 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2. doi:10.1074/jbc.RA119.011147
NLM
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
Vancouver
Sastre DE, Pulschen AA, Basso LGM, Pariente JSB, Marques Netto CGC, Machinandiarena F, Albanesi D, Navarro MV de AS, Mendoza D de, Gueiros Filho FJ. The phosphatidic acid pathway enzyme PlsX plays both catalytic and channeling roles in bacterial phospholipid synthesis [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2148-2159 + Supplementary materials Figs. S1-S5 and Tables S1 and S2.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011147
Artigo de periodico
Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium (2020)
Costa, Fernanda Rodrigues; Slivinski, Juliano ; Ióca, Laura Pavan ; Bertonha, Ariane Fernandes ; Felício, Rafael de; Cunha, Marcos Guilherme da; Madeira, Paulo Vinicius da Mata; Cauz, Ana C. G; Trindade, Daniel Maranho; Freire, Vitor F ; Ropke, Cristina Dislich; Gales, Ana; Brocchi, Marcelo; Ferreira, Antonio G; Gueiros Filho, Frederico José ; Trivella, Daniela Barretto Barbosa; Berlinck, Roberto Gomes de Souza ; Dessen, Andrea
Source: Bioorganic Chemistry. Unidades: IQ, IQSC
Assunto: PRODUTOS NATURAIS
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ABNT
COSTA, Fernanda Rodrigues et al. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium. Bioorganic Chemistry, v. 100, p. 1-8 art. 103921, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bioorg.2020.103921. Acesso em: 16 nov. 2024.
APA
Costa, F. R., Slivinski, J., Ióca, L. P., Bertonha, A. F., Felício, R. de, Cunha, M. G. da, et al. (2020). Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium. Bioorganic Chemistry, 100, 1-8 art. 103921. doi:10.1016/j.bioorg.2020.103921
NLM
Costa FR, Slivinski J, Ióca LP, Bertonha AF, Felício R de, Cunha MG da, Madeira PV da M, Cauz ACG, Trindade DM, Freire VF, Ropke CD, Gales A, Brocchi M, Ferreira AG, Gueiros Filho FJ, Trivella DBB, Berlinck RG de S, Dessen A. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium [Internet]. Bioorganic Chemistry. 2020 ; 100 1-8 art. 103921.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bioorg.2020.103921
Vancouver
Costa FR, Slivinski J, Ióca LP, Bertonha AF, Felício R de, Cunha MG da, Madeira PV da M, Cauz ACG, Trindade DM, Freire VF, Ropke CD, Gales A, Brocchi M, Ferreira AG, Gueiros Filho FJ, Trivella DBB, Berlinck RG de S, Dessen A. Merulinic acid C overcomes gentamicin resistance in Enterococcus faecium [Internet]. Bioorganic Chemistry. 2020 ; 100 1-8 art. 103921.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bioorg.2020.103921
Artigo de periodico
Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria (2020)
Sastre, Diego Emiliano; Basso, Luís Guilherme Mansor; Trastoy, Beatriz; Cifuente, Javier O.; Contreras, Xabier; Gueiros Filho, Frederico José ; Mendoza, Diego de; Navarro, Marcos Vicente de Albuquerque Salles ; Guerin, Marcelo E.
Source: Journal of Biological Chemistry. Unidades: IQ, IFSC, FFCLRP
Subjects: FOSFOLIPÍDEOS, LIPÍDEOS
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ABNT
SASTRE, Diego Emiliano et al. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, v. 295, n. 7, p. 2136-2147 + Supplementary materials Figs. S1-S9, 2020Tradução . . Disponível em: https://doi.org/10.1074/jbc.RA119.011122. Acesso em: 16 nov. 2024.
APA
Sastre, D. E., Basso, L. G. M., Trastoy, B., Cifuente, J. O., Contreras, X., Gueiros Filho, F. J., et al. (2020). Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria. Journal of Biological Chemistry, 295( 7), 2136-2147 + Supplementary materials Figs. S1-S9. doi:10.1074/jbc.RA119.011122
NLM
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011122
Vancouver
Sastre DE, Basso LGM, Trastoy B, Cifuente JO, Contreras X, Gueiros Filho FJ, Mendoza D de, Navarro MV de AS, Guerin ME. Membrane fluidity adjusts the insertion of the transacylase PlsX to regulate phospholipid biosynthesis in Gram-positive bacteria [Internet]. Journal of Biological Chemistry. 2020 ; 295( 7): 2136-2147 + Supplementary materials Figs. S1-S9.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1074/jbc.RA119.011122
Artigo de periodico
CALX-CBD1 Ca2+-Binding Cooperativity Studied by NMR Spectroscopy and ITC with Bayesian Statistics (2020)
Cardoso, Marcus ; Echeverri, Jose David Rivera ; Vitale, Phelipe A. M.; Degenhardt, Maximilia F. S.; Abiko, Layara A.; Oliveira, Cristiano ; Salinas, Roberto Kopke
Source: Biophysical Journal. Unidades: IF, IQ
Subjects: BIOFÍSICA, FÍSICO-QUÍMICA, DROSOPHILA, SENSORES QUÍMICOS, CÁLCIO, CRISTALOGRAFIA QUÍMICA, LIGAÇÕES QUÍMICAS
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ABNT
CARDOSO, Marcus et al. CALX-CBD1 Ca2+-Binding Cooperativity Studied by NMR Spectroscopy and ITC with Bayesian Statistics. Biophysical Journal, v. 119, n. 2, p. 337-348, 2020Tradução . . Disponível em: https://doi.org/10.1016/j.bpj.2020.05.031. Acesso em: 16 nov. 2024.
APA
Cardoso, M., Echeverri, J. D. R., Vitale, P. A. M., Degenhardt, M. F. S., Abiko, L. A., Oliveira, C., & Salinas, R. K. (2020). CALX-CBD1 Ca2+-Binding Cooperativity Studied by NMR Spectroscopy and ITC with Bayesian Statistics. Biophysical Journal, 119( 2), 337-348. doi:10.1016/j.bpj.2020.05.031
NLM
Cardoso M, Echeverri JDR, Vitale PAM, Degenhardt MFS, Abiko LA, Oliveira C, Salinas RK. CALX-CBD1 Ca2+-Binding Cooperativity Studied by NMR Spectroscopy and ITC with Bayesian Statistics [Internet]. Biophysical Journal. 2020 ; 119( 2): 337-348.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bpj.2020.05.031
Vancouver
Cardoso M, Echeverri JDR, Vitale PAM, Degenhardt MFS, Abiko LA, Oliveira C, Salinas RK. CALX-CBD1 Ca2+-Binding Cooperativity Studied by NMR Spectroscopy and ITC with Bayesian Statistics [Internet]. Biophysical Journal. 2020 ; 119( 2): 337-348.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.bpj.2020.05.031
Artigo de periodico
Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite (2017)
Alegria, Thiago Gerônimo Pires; Meireles, Diogo A; Cussiol, José R. R; Hugo, Martins; Trujillo, Madia; Oliveira, Marcos Antônio de; Miyamoto, Sayuri ; Queiroz, Raphael F; Valadares, Napoleão Fonseca; Garratt, Richard Charles ; Radi, Rafael; Di Mascio, Paolo ; Augusto, Ohara ; Netto, Luis Eduardo Soares
Source: Proceedings of the National Academy of Sciences of the United States of America - PNAS. Unidades: IB, IQ, IFSC
Subjects: BACTÉRIAS PATOGÊNICAS, PSEUDOMONAS, ÁCIDOS GRAXOS
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ABNT
ALEGRIA, Thiago Gerônimo Pires et al. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite. Proceedings of the National Academy of Sciences of the United States of America - PNAS, v. 114, n. Ja 2017, p. E132-E141 + supplementary materials: S1-S6, 2017Tradução . . Disponível em: https://doi.org/10.1073/pnas.1619659114. Acesso em: 16 nov. 2024.
APA
Alegria, T. G. P., Meireles, D. A., Cussiol, J. R. R., Hugo, M., Trujillo, M., Oliveira, M. A. de, et al. (2017). Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite. Proceedings of the National Academy of Sciences of the United States of America - PNAS, 114( Ja 2017), E132-E141 + supplementary materials: S1-S6. doi:10.1073/pnas.1619659114
NLM
Alegria TGP, Meireles DA, Cussiol JRR, Hugo M, Trujillo M, Oliveira MA de, Miyamoto S, Queiroz RF, Valadares NF, Garratt RC, Radi R, Di Mascio P, Augusto O, Netto LES. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2017 ; 114( Ja 2017): E132-E141 + supplementary materials: S1-S6.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1073/pnas.1619659114
Vancouver
Alegria TGP, Meireles DA, Cussiol JRR, Hugo M, Trujillo M, Oliveira MA de, Miyamoto S, Queiroz RF, Valadares NF, Garratt RC, Radi R, Di Mascio P, Augusto O, Netto LES. Ohr plays a central role in bacterial responses against fatty acid hydroperoxides and peroxynitrite [Internet]. Proceedings of the National Academy of Sciences of the United States of America - PNAS. 2017 ; 114( Ja 2017): E132-E141 + supplementary materials: S1-S6.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1073/pnas.1619659114
Artigo de periodico
Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum (2017)
Florindo, Renata Nóbrega; Souza, Valquiria Pianheri; Mutti, Hemily S.; Camilo, César Moisés; Manzine, Livia Regina; Marana, Sandro Roberto ; Polikarpov, Igor ; Nascimento, Alessandro Silva
Source: New Biotechnology. Unidades: IFSC, IQ
Subjects: TRICHODERMA, ENZIMAS
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ABNT
FLORINDO, Renata Nóbrega et al. Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum. New Biotechnology, v. 40, n. Ja 2017, p. 218-227, 2017Tradução . . Disponível em: https://doi.org/10.1016/j.nbt.2017.08.012. Acesso em: 16 nov. 2024.
APA
Florindo, R. N., Souza, V. P., Mutti, H. S., Camilo, C. M., Manzine, L. R., Marana, S. R., et al. (2017). Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum. New Biotechnology, 40( Ja 2017), 218-227. doi:10.1016/j.nbt.2017.08.012
NLM
Florindo RN, Souza VP, Mutti HS, Camilo CM, Manzine LR, Marana SR, Polikarpov I, Nascimento AS. Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum [Internet]. New Biotechnology. 2017 ; 40( Ja 2017): 218-227.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.nbt.2017.08.012
Vancouver
Florindo RN, Souza VP, Mutti HS, Camilo CM, Manzine LR, Marana SR, Polikarpov I, Nascimento AS. Structural insights into β-glucosidase transglycosylation based on biochemical, structural and computational analysis of two GH1 enzymes from Trichoderma harzianum [Internet]. New Biotechnology. 2017 ; 40( Ja 2017): 218-227.[citado 2024 nov. 16 ] Available from: https://doi.org/10.1016/j.nbt.2017.08.012

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